CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012336
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 DNA replication licensing factor MCM6 
Protein Synonyms/Alias
 p105MCM 
Gene Name
 MCM6 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
28EVAEKCQKLFLDFLEubiquitination[1]
95PYLCRALKTFVKDRKubiquitination[1]
102KTFVKDRKEIPLAKDubiquitination[1, 2]
108RKEIPLAKDFYVAFQubiquitination[3, 4, 5, 6]
173RDVEQQFKYTQPNICubiquitination[1, 2, 4]
197RFLLDTNKSRFVDFQubiquitination[1, 2, 3, 4, 5, 6, 7]
205SRFVDFQKVRIQETQubiquitination[1, 3, 4, 5, 6, 7]
241ESAQAGDKCDFTGTLubiquitination[1]
256IVVPDVSKLSTPGARubiquitination[1]
313TNPRFGGKELRDEEQubiquitination[1, 2, 4, 5, 8]
326EQTAESIKNQMTVKEubiquitination[1, 2, 4]
332IKNQMTVKEWEKVFEubiquitination[1, 2, 3, 4, 6, 9]
344VFEMSQDKNLYHNLCubiquitination[1]
365IHGNDEVKRGVLLMLubiquitination[2]
402VGDPSTAKSQFLKHVubiquitination[1, 2]
407TAKSQFLKHVEEFSPacetylation[10]
407TAKSQFLKHVEEFSPubiquitination[1, 2, 3, 4, 5, 6, 7]
422RAVYTSGKASSAAGLubiquitination[1, 2, 3, 4, 5, 6, 7, 8, 9, 11]
486QQTISITKAGVKATLubiquitination[1, 2, 3, 4, 5, 6, 7]
490SITKAGVKATLNARTubiquitination[1, 2, 4, 5]
517YDRSKSLKQNINLSAubiquitination[1, 2, 3, 4, 5, 6, 7, 8, 9, 11]
588QFKPKISKESEDFIVubiquitination[1, 2, 4]
599DFIVEQYKHLRQRDGacetylation[2, 12]
599DFIVEQYKHLRQRDGubiquitination[1, 2, 3, 6, 9]
611RDGSGVTKSSWRITVubiquitination[1, 2, 4, 5, 7, 8]
643CCDEVQPKHVKEAFRacetylation[2, 12]
643CCDEVQPKHVKEAFRubiquitination[1, 2, 4, 7]
646EVQPKHVKEAFRLLNacetylation[2]
646EVQPKHVKEAFRLLNubiquitination[1]
654EAFRLLNKSIIRVETubiquitination[1, 3, 4, 5, 6]
733LIVLHLRKVEEEEDEubiquitination[2, 4, 5]
744EEDESALKRSELVNWubiquitination[2, 4, 5, 11]
769SEEELINKKRIIEKVubiquitination[4]
775NKKRIIEKVIHRLTHacetylation[12]
775NKKRIIEKVIHRLTHubiquitination[1, 2, 3, 4, 6, 9]
796ELTQAGLKGSTEGSEubiquitination[4, 5, 11]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [3] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [4] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [5] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [6] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [7] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [8] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [9] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [10] Monoclonal antibody cocktail as an enrichment tool for acetylome analysis.
 Shaw PG, Chaerkady R, Zhang Z, Davidson NE, Pandey A.
 Anal Chem. 2011 May 15;83(10):3623-6. [PMID: 21466224]
 [11] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [12] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861] 
Functional Description
 Acts as component of the MCM2-7 complex (MCM complex) which is the putative replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity. 
Sequence Annotation
 DOMAIN 346 553 MCM.
 NP_BIND 396 403 ATP (Potential).
 MOTIF 528 531 Arginine finger.
 MOD_RES 1 1 N-acetylmethionine.
 MOD_RES 13 13 Phosphoserine.
 MOD_RES 271 271 Phosphoserine.
 MOD_RES 762 762 Phosphoserine.
 MOD_RES 791 791 Phosphothreonine.  
Keyword
 3D-structure; Acetylation; ATP-binding; Cell cycle; Complete proteome; DNA replication; DNA-binding; Glycoprotein; Helicase; Hydrolase; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 821 AA 
Protein Sequence
MDLAAAAEPG AGSQHLEVRD EVAEKCQKLF LDFLEEFQSS DGEIKYLQLA EELIRPERNT 60
LVVSFVDLEQ FNQQLSTTIQ EEFYRVYPYL CRALKTFVKD RKEIPLAKDF YVAFQDLPTR 120
HKIRELTSSR IGLLTRISGQ VVRTHPVHPE LVSGTFLCLD CQTVIRDVEQ QFKYTQPNIC 180
RNPVCANRRR FLLDTNKSRF VDFQKVRIQE TQAELPRGSI PRSLEVILRA EAVESAQAGD 240
KCDFTGTLIV VPDVSKLSTP GARAETNSRV SGVDGYETEG IRGLRALGVR DLSYRLVFLA 300
CCVAPTNPRF GGKELRDEEQ TAESIKNQMT VKEWEKVFEM SQDKNLYHNL CTSLFPTIHG 360
NDEVKRGVLL MLFGGVPKTT GEGTSLRGDI NVCIVGDPST AKSQFLKHVE EFSPRAVYTS 420
GKASSAAGLT AAVVRDEESH EFVIEAGALM LADNGVCCID EFDKMDVRDQ VAIHEAMEQQ 480
TISITKAGVK ATLNARTSIL AAANPISGHY DRSKSLKQNI NLSAPIMSRF DLFFILVDEC 540
NEVTDYAIAR RIVDLHSRIE ESIDRVYSLD DIRRYLLFAR QFKPKISKES EDFIVEQYKH 600
LRQRDGSGVT KSSWRITVRQ LESMIRLSEA MARMHCCDEV QPKHVKEAFR LLNKSIIRVE 660
TPDVNLDQEE EIQMEVDEGA GGINGHADSP APVNGINGYN EDINQESAPK ASLRLGFSEY 720
CRISNLIVLH LRKVEEEEDE SALKRSELVN WYLKEIESEI DSEEELINKK RIIEKVIHRL 780
THYDHVLIEL TQAGLKGSTE GSESYEEDPY LVVNPNYLLE D 821 
Gene Ontology
 GO:0042555; C:MCM complex; IDA:UniProtKB.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0005524; F:ATP binding; NAS:UniProtKB.
 GO:0003678; F:DNA helicase activity; IEA:Compara.
 GO:0003697; F:single-stranded DNA binding; IEA:Compara.
 GO:0006270; P:DNA replication initiation; IEA:InterPro.
 GO:0006271; P:DNA strand elongation involved in DNA replication; TAS:Reactome.
 GO:0006268; P:DNA unwinding involved in replication; IEA:Compara.
 GO:0000082; P:G1/S transition of mitotic cell cycle; TAS:Reactome. 
Interpro
 IPR008049; MCM6.
 IPR018525; MCM_CS.
 IPR001208; MCM_DNA-dep_ATPase.
 IPR012340; NA-bd_OB-fold.
 IPR027417; P-loop_NTPase.
 IPR004039; Rubredoxin-type_fold. 
Pfam
 PF00493; MCM 
SMART
 SM00350; MCM 
PROSITE
 PS00847; MCM_1
 PS50051; MCM_2 
PRINTS
 PR01657; MCMFAMILY.
 PR01662; MCMPROTEIN6.